Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy

Autoři: Frauke Beilstein aff001;  Gary H. Cohen aff002;  Roselyn J. Eisenberg aff003;  Valérie Nicolas aff004;  Audrey Esclatine aff001;  David Pasdeloup aff001
Působiště autorů: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris‐Sud, Université Paris‐Saclay, Gif‐sur‐Yvette cedex, France aff001;  Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America aff002;  Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America aff003;  IPSIT, Microscopy facility, University of Paris-Sud, Châtenay-Malabry, France aff004;  Laboratory of Biology of Avian Viruses, UMR1282 ISP, INRA Centre Val-de-Loire, Nouzilly, France aff005
Vyšlo v časopise: Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy. PLoS Pathog 15(12): e32767. doi:10.1371/journal.ppat.1008209
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.ppat.1008209


The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins must be located at the point of contact between cellular and viral envelopes to interact and allow fusion. Using super-resolution microscopy, we show that gB, gH/gL and most of gC are distributed evenly round purified virions. In contrast, gD localizes essentially as clusters which are distinct from gB and gH/gL. Upon cell binding, we observe that all glycoproteins, including gD, have a similar ring-like pattern, but the diameter of these rings was significantly smaller than those observed on cell-free viruses. We also observe that contrary to cell-free particles, gD mostly colocalizes with other glycoproteins on cell-bound particles. The differing patterns of localization of gD between cell-free and cell-bound viruses indicates that gD can be reorganized on the viral envelope following either a possible maturation of the viral particle or its adsorption to the cell. This redistribution of glycoproteins upon cell attachment could contribute to initiate the cascade of activations leading to membrane fusion.

Klíčová slova:

Antibodies – Cell binding – Glycoproteins – Membrane fusion – Viral packaging – Virions – Virus glycoproteins – Viral envelope


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